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Entry version 103 (18 Sep 2019)
Sequence version 1 (31 Oct 2006)
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Protein

Genome polyprotein

Gene
N/A
Organism
Yellow fever virus (isolate Ethiopia/Couma/1961) (YFV)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Protein inferred from homologyi <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Capsid protein C: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions.By similarity
Capsid protein C: Inhibits RNA silencing by interfering with host Dicer.By similarity
Peptide pr: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers.By similarity
Protein prM: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.By similarity
Small envelope protein M: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity.By similarity
Envelope protein E: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.By similarity
Non-structural protein 1: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3).By similarity
Non-structural protein 2A: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.By similarity
Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity).PROSITE-ProRule annotationBy similarity
Serine protease NS3: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction. Also plays a role in virus assembly (By similarity).PROSITE-ProRule annotationBy similarity
Non-structural protein 4A: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding.By similarity
Peptide 2k: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.By similarity
Non-structural protein 4B: Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway.By similarity
RNA-directed RNA polymerase NS5: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala. EC:3.4.21.91

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1537Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1561Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1622Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei1945Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1948Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei2520mRNA cap bindingPROSITE-ProRule annotation1
Sitei2523mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2524mRNA cap bindingPROSITE-ProRule annotation1
Sitei2526mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2531mRNA cap bindingPROSITE-ProRule annotation1
Sitei2535mRNA cap bindingPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei2563S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2568For 2'-O-MTase activityBy similarity1
Sitei2568Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2593S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2594S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2611S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2612S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2638S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2639S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2653For 2'-O-MTase activityBy similarity1
Sitei2653Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2654S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2657mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2689For 2'-O-MTase activityBy similarity1
Sitei2689Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Sitei2720mRNA cap bindingPROSITE-ProRule annotation1
Sitei2722mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2725For 2'-O-MTase activityBy similarity1
Sitei2725Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2727S-adenosyl-L-methioninePROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi2946Zinc 1By similarity1
Metal bindingi2950Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2955Zinc 1By similarity1
Metal bindingi2958Zinc 1By similarity1
Metal bindingi3223Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3239Zinc 2By similarity1
Metal bindingi3358Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1682 – 1689ATPPROSITE-ProRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHelicase, Hydrolase, Methyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Serine protease, Suppressor of RNA silencing, Transferase
Biological processActivation of host autophagy by virus, Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host STAT2 by virus, mRNA capping, mRNA processing, Transcription, Transcription regulation, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell
LigandATP-binding, GTP-binding, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine, Zinc

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 14 chains:
Alternative name(s):
Core protein
Alternative name(s):
Matrix protein
Non-structural protein 2A-alpha
Short name:
NS2A-alpha
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Serine protease NS3 (EC:3.4.21.91, EC:3.6.1.15By similarity, EC:3.6.4.13By similarity)
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
RNA-directed RNA polymerase NS5 (EC:2.1.1.56PROSITE-ProRule annotation, EC:2.1.1.57PROSITE-ProRule annotation, EC:2.7.7.48PROSITE-ProRule annotation)
Alternative name(s):
Non-structural protein 5
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiYellow fever virus (isolate Ethiopia/Couma/1961) (YFV)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri407141 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesRiboviriaFlaviviridaeFlavivirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiAedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159]
Aedes luteocephalus (Mosquito) [TaxID: 299629]
Aedes simpsoni [TaxID: 7161]
Homo sapiens (Human) [TaxID: 9606]
Simiiformes [TaxID: 314293]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000008604 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Capsid protein C :
Peptide pr :
Small envelope protein M :
Envelope protein E :
Non-structural protein 1 :
Non-structural protein 2A :
Serine protease NS3 :
Non-structural protein 4A :
Non-structural protein 4B :
RNA-directed RNA polymerase NS5 :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 104CytoplasmicSequence analysisAdd BLAST104
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei105 – 125HelicalSequence analysisAdd BLAST21
Topological domaini126 – 244ExtracellularSequence analysisAdd BLAST119
Transmembranei245 – 265HelicalSequence analysisAdd BLAST21
Topological domaini266 – 270CytoplasmicSequence analysis5
Transmembranei271 – 285HelicalSequence analysisAdd BLAST15
Topological domaini286 – 730ExtracellularSequence analysisAdd BLAST445
Transmembranei731 – 751HelicalSequence analysisAdd BLAST21
Topological domaini752 – 757ExtracellularSequence analysis6
Transmembranei758 – 778HelicalSequence analysisAdd BLAST21
Topological domaini779 – 1132ExtracellularBy similarityAdd BLAST354
Transmembranei1133 – 1153HelicalBy similarityAdd BLAST21
Topological domaini1154 – 1201CytoplasmicBy similarityAdd BLAST48
Transmembranei1202 – 1222HelicalBy similarityAdd BLAST21
Topological domaini1223 – 1287LumenalBy similarityAdd BLAST65
Transmembranei1288 – 1308HelicalBy similarityAdd BLAST21
Topological domaini1309 – 1355CytoplasmicBy similarityAdd BLAST47
Transmembranei1356 – 1376HelicalBy similarityAdd BLAST21
Topological domaini1377 – 1378LumenalBy similarity2
Transmembranei1379 – 1399HelicalSequence analysisAdd BLAST21
Topological domaini1400 – 1456CytoplasmicSequence analysisAdd BLAST57
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei1457 – 1477HelicalSequence analysisAdd BLAST21
Topological domaini1478 – 2157CytoplasmicSequence analysisAdd BLAST680
Transmembranei2158 – 2178HelicalSequence analysisAdd BLAST21
Topological domaini2179 – 2186LumenalSequence analysis8
Intramembranei2187 – 2207HelicalSequence analysisAdd BLAST21
Topological domaini2208 – 2209LumenalSequence analysis2
Transmembranei2210 – 2230HelicalSequence analysisAdd BLAST21
Topological domaini2231 – 2241CytoplasmicSequence analysisAdd BLAST11
Transmembranei2242 – 2262Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2263 – 2293LumenalSequence analysisAdd BLAST31
Intramembranei2294 – 2314HelicalSequence analysisAdd BLAST21
Topological domaini2315 – 2360LumenalSequence analysisAdd BLAST46
Transmembranei2361 – 2380HelicalSequence analysisAdd BLAST20
Topological domaini2381 – 2421CytoplasmicSequence analysisAdd BLAST41
Transmembranei2422 – 2442HelicalSequence analysisAdd BLAST21
Topological domaini2443 – 2445LumenalSequence analysis3
Transmembranei2446 – 2466HelicalSequence analysisAdd BLAST21
Topological domaini2467 – 3411CytoplasmicSequence analysisAdd BLAST945

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host endoplasmic reticulum, Host membrane, Host nucleus, Membrane, Secreted, Viral envelope protein, Virion

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004051621 – 3412Genome polyproteinAdd BLAST3412
ChainiPRO_00002615601 – 101Capsid protein CBy similarityAdd BLAST101
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000261561102 – 121ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST20
ChainiPRO_0000261562122 – 285Protein prMBy similarityAdd BLAST164
ChainiPRO_0000261563122 – 210Peptide prBy similarityAdd BLAST89
ChainiPRO_0000261564211 – 285Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000261565286 – 778Envelope protein EBy similarityAdd BLAST493
ChainiPRO_0000261566779 – 1130Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00002615671131 – 1354Non-structural protein 2ABy similarityAdd BLAST224
ChainiPRO_00002615681131 – 1320Non-structural protein 2A-alphaBy similarityAdd BLAST190
ChainiPRO_00002615691355 – 1484Serine protease subunit NS2BBy similarityAdd BLAST130
ChainiPRO_00002615701485 – 2107Serine protease NS3By similarityAdd BLAST623
ChainiPRO_00002615712108 – 2233Non-structural protein 4ABy similarityAdd BLAST126
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_00002615722234 – 2256Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00002615732257 – 2507Non-structural protein 4BBy similarityAdd BLAST251
ChainiPRO_00002615742508 – 3412RNA-directed RNA polymerase NS5By similarityAdd BLAST905

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi134N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi150N-linked (GlcNAc...) asparagine; by hostSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi288 ↔ 315By similarity
Disulfide bondi345 ↔ 406By similarity
Disulfide bondi345 ↔ 401By similarity
Disulfide bondi359 ↔ 390By similarity
Disulfide bondi377 ↔ 406By similarity
Disulfide bondi377 ↔ 401By similarity
Disulfide bondi467 ↔ 568By similarity
Disulfide bondi585 ↔ 615By similarity
Disulfide bondi782 ↔ 793By similarity
Disulfide bondi833 ↔ 921By similarity
Glycosylationi908N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi957 ↔ 1002By similarity
Glycosylationi986N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi1058 ↔ 1107By similarity
Disulfide bondi1069 ↔ 1091By similarity
Disulfide bondi1090 ↔ 1094By similarity
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2563PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Genome polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. The nascent capsid protein C contains a C-terminal hydrophobic domain that act as a signal sequence for translocation of prM into the lumen of the ER. Mature capsid protein C is cleaved at a site upstream of this hydrophobic domain by NS3. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. Non-structural protein 2A-alpha, a C-terminally truncated form of non-structural protein 2A, results from partial cleavage by NS3. Specific enzymatic cleavages in vivo yield mature proteins peptide 2K acts as a signal sequence and is removed from the N-terminus of NS4B by the host signal peptidase in the ER lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.By similarity
Protein prM: Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM.By similarity
Envelope protein E: N-glycosylated.By similarity
Non-structural protein 1: N-glycosylated. The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells.By similarity
Polyubiquitinated; ubiquitination is probably mediated by host TRIM23 and is prerequisite for NS5-STAT2 interaction. NS5 is not ISGylated or sumoylated.By similarity
RNA-directed RNA polymerase NS5: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei101 – 102Cleavage; by viral protease NS3By similarity2
Sitei121 – 122Cleavage; by host signal peptidaseBy similarity2
Sitei210 – 211Cleavage; by host furinBy similarity2
Sitei285 – 286Cleavage; by host signal peptidaseBy similarity2
Sitei778 – 779Cleavage; by host signal peptidaseBy similarity2
Sitei1130 – 1131Cleavage; by hostBy similarity2
Sitei1354 – 1355Cleavage; by viral protease NS3By similarity2
Sitei1484 – 1485Cleavage; by autolysisBy similarity2
Sitei2107 – 2108Cleavage; by autolysisBy similarity2
Sitei2233 – 2234Cleavage; by viral protease NS3By similarity2
Sitei2256 – 2257Cleavage; by host signal peptidaseBy similarity2
Sitei2507 – 2508Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q074N0

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Capsid protein C: Homodimer.

Interacts (via N-terminus) with host EXOC1 (via C-terminus); this interaction results in EXOC1 degradation through the proteasome degradation pathway. Protein prM: Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi. Envelope protein E: Homodimer; in the endoplasmic reticulum and Golgi.

Interacts with protein prM.

Interacts with non-structural protein 1. Non-structural protein 1: Homodimer; Homohexamer when secreted.

Interacts with envelope protein E. Non-structural protein 2A:

Interacts (via N-terminus) with serine protease NS3. Non-structural protein 2B:

Forms a heterodimer with serine protease NS3. May form homooligomers. Serine protease NS3:

Forms a heterodimer with NS2B.

Interacts with non-structural protein 2A (via N-terminus).

Interacts with NS4B.

Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity. NS3 interacts with host PDCD6IP; this interaction contributes to virion release. Non-structural protein 4B:

Interacts with serine protease NS3. RNA-directed RNA polymerase NS5: Homodimer.

Interacts with host STAT2; this interaction prevents the establishment of cellular antiviral state.

Interacts with host TRIM23; this interaction leads to NS5 ubiquitination.

By similarity

GO - Molecular functioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q074N0

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1485 – 1665Peptidase S7PROSITE-ProRule annotationAdd BLAST181
Domaini1669 – 1825Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1820 – 1997Helicase C-terminalAdd BLAST178
Domaini2508 – 2772mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST265
Domaini3036 – 3188RdRp catalyticPROSITE-ProRule annotationAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni38 – 72Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST35
Regioni383 – 396Fusion peptideBy similarityAdd BLAST14
Regioni1407 – 1446Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1673 – 1676Important for RNA-bindingBy similarity4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1773 – 1776DEAH boxPROSITE-ProRule annotation4
Motifi2879 – 2912Nuclear localization signalBy similarityAdd BLAST34

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi2153 – 2201Met-richAdd BLAST49

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The transmembrane domains of the small envelope protein M and envelope protein E contain an endoplasmic reticulum retention signal.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

In the N-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type methyltransferase family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Conserved Domains Database

More...
CDDi
cd12149 Flavi_E_C, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.8.970, 1 hit
1.20.1280.260, 1 hit
2.60.260.50, 1 hit
2.60.40.350, 1 hit
2.60.98.10, 1 hit
3.30.387.10, 1 hit
3.30.67.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011492 DEAD_Flavivir
IPR000069 Env_glycoprot_M_flavivir
IPR038302 Env_glycoprot_M_sf_flavivir
IPR013755 Flav_gly_cen_dom_subdom1
IPR001122 Flavi_capsidC
IPR027287 Flavi_E_Ig-like
IPR026470 Flavi_E_Stem/Anchor_dom
IPR038345 Flavi_E_Stem/Anchor_dom_sf
IPR001157 Flavi_NS1
IPR000752 Flavi_NS2A
IPR000487 Flavi_NS2B
IPR000404 Flavi_NS4A
IPR001528 Flavi_NS4B
IPR002535 Flavi_propep
IPR038688 Flavi_propep_sf
IPR000336 Flavivir/Alphavir_Ig-like_sf
IPR001850 Flavivirus_NS3_S7
IPR014412 Gen_Poly_FLV
IPR011998 Glycoprot_cen/dimer
IPR036253 Glycoprot_cen/dimer_sf
IPR038055 Glycoprot_E_dimer_dom
IPR013756 GlyE_cen_dom_subdom2
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR014756 Ig_E-set
IPR026490 mRNA_cap_0/1_MeTrfase
IPR027417 P-loop_NTPase
IPR009003 Peptidase_S1_PA
IPR000208 RNA-dir_pol_flavivirus
IPR007094 RNA-dir_pol_PSvirus
IPR002877 rRNA_MeTrfase_FtsJ_dom
IPR029063 SAM-dependent_MTases

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01003 Flavi_capsid, 1 hit
PF07652 Flavi_DEAD, 1 hit
PF02832 Flavi_glycop_C, 1 hit
PF00869 Flavi_glycoprot, 1 hit
PF01004 Flavi_M, 1 hit
PF00948 Flavi_NS1, 1 hit
PF01005 Flavi_NS2A, 1 hit
PF01002 Flavi_NS2B, 1 hit
PF01350 Flavi_NS4A, 1 hit
PF01349 Flavi_NS4B, 1 hit
PF00972 Flavi_NS5, 1 hit
PF01570 Flavi_propep, 1 hit
PF01728 FtsJ, 1 hit
PF00949 Peptidase_S7, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF003817 Gen_Poly_FLV, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 2 hits
SSF53335 SSF53335, 1 hit
SSF56983 SSF56983, 1 hit
SSF81296 SSF81296, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR04240 flavi_E_stem, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51527 FLAVIVIRUS_NS2B, 1 hit
PS51528 FLAVIVIRUS_NS3PRO, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit
PS51591 RNA_CAP01_NS5_MT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q074N0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGRKAQGKT LGVNMVRRGA RSLSNKIKQK TKQIGNRPGP SRGVQGFIFF
60 70 80 90 100
FLFNILTGKK LTTHLKRLWR MLDPRQGLAV LRKVKRVVAS LMIGLSSRKR
110 120 130 140 150
RSNEMAMMPL LILSMVILAG GVTLVRKNRW LLLNVTAEDL GKTFSLGTGN
160 170 180 190 200
CTTNILEAKY WCPDSMEYNC PNLSPREEPD DIDCWCYGVE NVRVAYGRCD
210 220 230 240 250
AVGRSKRSRR AIDLPTHENH GLKTRQEKWM AGRMGERQLQ KIERWLVRNP
260 270 280 290 300
FFAITALAIA YLVGNNMTQR VVIALLVLAV GPAYSAHCIG ITDRDFIEGV
310 320 330 340 350
HGGTWVSATL EQGKCVTVMA PDKPSLDISL QTVAIDGPAE ARKVCYSAVL
360 370 380 390 400
THVKINDKCP STGEAHLAEE NDGDNACKRT YSDRGWGNGC GLFGKGSIVA
410 420 430 440 450
CAKFTCAKSM SLFEVDQTKI QYVIRAQLHV GAKQENWNTD IKTLKFDALS
460 470 480 490 500
GSQEAEFTGY GKATLECQVQ TAVDFGNSYI AEMEKDSWIV DRQWAQDLTL
510 520 530 540 550
PWQSGSGGIW REMHHLVEFE PPHAATIRVL ALGNQEGSLK TALTGAMRVT
560 570 580 590 600
KDENDNNLYK LHGGHVSCRV KLSALTLKGT SYKMCTDKMS FVKNPTDTGH
610 620 630 640 650
GTVVMQVKVP KGAPCKIPVI VADDLTAAVN KGILVTVNPI ASTNDDEVLI
660 670 680 690 700
EVNPPFGDSY IIVGTGDSRL TYQWHKEGSS IGKLFTQTMK GAERLAVMGD
710 720 730 740 750
AAWDFSSAGG FFTSVGKGIH TVFGSAFQGL FGGLSWITKV IMGAVLIWVG
760 770 780 790 800
INTRNMTMSM SMILVGVIMM FLSLGVGADQ GCAVNFGKRE LKCGDGIFVF
810 820 830 840 850
RDSDDWLTKY SYYPEDPVKL ASIIKASHEE GKCGLNSVDS LEHEMWRSRA
860 870 880 890 900
DEINAIFEEN EVDISVVVQD PKNIYQRGTH PFSRIRDGLQ YGWKTWGKNL
910 920 930 940 950
IFSPGRKNGS FIIDGKSRKE CPFSNRVWNS FQIEEFGMGV FTTRVFMDAV
960 970 980 990 1000
FDYSVDCDGA ILGAAVNGKK SAHGSPTFWM GSHEVNGTWM VHTLETLDYK
1010 1020 1030 1040 1050
ECEWPLTHTI GTSVEESDMF MPRSIGGPVS SHNHIPGYKV QTNGPWMQVP
1060 1070 1080 1090 1100
LEVRREPCPG TSVVLDTGCD GRGKSTRSTT DSGKIIPEWC CRSCTMPPVS
1110 1120 1130 1140 1150
FHGSDGCWYP MEIRPMKTHE SHLVRSWVTA GEVHAVPFGL VSMMIAMEVV
1160 1170 1180 1190 1200
LRKRQGPKQM LVGGIILLGA MLVGQVTVLD LVKLIVAVGL HFHEINNGGD
1210 1220 1230 1240 1250
AMYMALIASF SIRPGLLVGF GLRTLWSPRE RLVMAFGAAM VEVALGGMMG
1260 1270 1280 1290 1300
GLWQYLNAVS LCVLTINAIS SRKASNAVLP LMALLTPVTM HEVRMATMLF
1310 1320 1330 1340 1350
CTVVIVGVLH QNAKDTSMQK TIPIVALTLT SYMGLTQPFL GLCAYMSTQV
1360 1370 1380 1390 1400
FGRRSIPVNE ALAAAGLVGV LAGLAFQDME NFLGPIAVGG ILMMLVSVAG
1410 1420 1430 1440 1450
KVDGLELKKL GEVSWEEEAE ISGSSSRYDV ALSEQGEFKL LSEDKVPWDQ
1460 1470 1480 1490 1500
IVMTSLALVG AAIHPFALLL VLGGWVLHIK GARRSGDVLW DIPTPKVIEE
1510 1520 1530 1540 1550
CEYLEDGIYG IFQSTFLGAS QRGVGVAQGG VFHTMWHVTR GAFLLRNGKK
1560 1570 1580 1590 1600
LVPSWASVKE DLVAYGGSWK LDGKWDGEEE VQLIAAVPGK AVVNVQTKPS
1610 1620 1630 1640 1650
VFKVRNGGEI GAVALDYPSG TSGSPIVNRS GEVVGLYGNG ILVGDNSFVS
1660 1670 1680 1690 1700
AISQTEVKEE SKEELQEIPT MLKKGMTTIL DFHPGAGKTR RFLPQILAEC
1710 1720 1730 1740 1750
ARRRLRTLVL APTRVVLSEM KEAFHGLDVK FHTQAFSAHG SGKEVIDAMC
1760 1770 1780 1790 1800
HATLTYRMLE PTRAVNWEVI IMDEAHFLDP ASIAARGWAA HRARANESAT
1810 1820 1830 1840 1850
ILMTATPPGT SDEFPHSNGE IEDVQTDIPS EPWTSGHEWI LADKRPTAWF
1860 1870 1880 1890 1900
LPSIRAANVM AASLRKAGKS VVVLNRKTFE KEYPTIKQKR PDFILATDIA
1910 1920 1930 1940 1950
EMGANLCVER VLDCRTAYKP VLVDEGRKVA IKGPLRISAS SAAQRRGRIG
1960 1970 1980 1990 2000
RNPNRDGDSY YYSEPTSEDN AHHVCWLEAS MLLDNMEVRG GMVAPLYGIE
2010 2020 2030 2040 2050
GTKTPVSPGE MRLRDDQRRV FRELVRGCDL PVWLSWQVAK PGLKTNDRKW
2060 2070 2080 2090 2100
CFEGPEEHEI LNDNGETVKC RSPGGAKKAL RPRWCDERVS SDQSALADFI
2110 2120 2130 2140 2150
KFAEGRRGAA EMLVVLTELP DFLAKKGGEA MDTISVFLHS EEGSRAYRNA
2160 2170 2180 2190 2200
LSMMPEAMTI VMLFILAGLL TSGMVIFFMS PKGMSRMSMA MGTMAGSGYL
2210 2220 2230 2240 2250
MFLGGVKPTH ISYVMLIFFV LMVVIIPEPG QQRTIQDNQV AYLIIGILTL
2260 2270 2280 2290 2300
LSIVAANELG MLEKTKEDFF GRRNIATSGG TIPWSWPDLD LKPGAAWTVY
2310 2320 2330 2340 2350
VGIVTMLSPM LHHWIKVEYG NLSLSGIAQS ASVLSFMDKG IPFMKMNISV
2360 2370 2380 2390 2400
VILLVSGWNS ITVIPLLCGV GGAMLHWTLI LPGIKAQQSK LAQKRVFHGV
2410 2420 2430 2440 2450
AKNPVVDGNP TADIEEAPEM PALYEKKLAL YLLLALSLMS VAMCRTPFSL
2460 2470 2480 2490 2500
AEGIVLSSAA LGPLIEGNTS LLWNGPMAVS MTGVMRGNYY AFVGVMYNLW
2510 2520 2530 2540 2550
KMKTGRRGSA SGKTLGEVWK RELNLLDKQQ FELYKRTDIT EVDRDMARRH
2560 2570 2580 2590 2600
LAEGKVDTGV AVSRGTAKLR WFHERGYVKL EGRVMDLGCG RGGWCYYAAA
2610 2620 2630 2640 2650
QKEVSGVKGY TLGRDGHEKP MNVQSLGWNI VTFKDKTDIH RLEPAKCETL
2660 2670 2680 2690 2700
LCDIGESSPS SVTEGERTLR VLETIEKWLA CGVDNFCVKV LAPYMPDVIE
2710 2720 2730 2740 2750
KLELLQRRFG GTIIRNPLSR NSTHEMYYVS GARSNITFTV NQTSRLLMRR
2760 2770 2780 2790 2800
MRRPTGKVTL EPDVILPIGT RSVETDKGPL DRDAIEERVE RIKTEYAATW
2810 2820 2830 2840 2850
FYDNDNPYRT WHYCGSYITK TSGSAASMIN GVIKILTFPW DRIEEVTRMA
2860 2870 2880 2890 2900
MTDTTPFGQQ RVFKEKVDTR AKDPPAGTRK IMKVVNRWLF RHLAREKNPR
2910 2920 2930 2940 2950
LCTKEEFIAK VRSHAAVGAF LEEQEQWKTA NEAVQDPKFW EMVDAERKLH
2960 2970 2980 2990 3000
QQGRCQSCVY NMMGKREKKL SEFGKAKGSR AIWYMWLGAR FLEFEALGFL
3010 3020 3030 3040 3050
NEDHWASREN SGGGVEGIGL QYLGYVIKDL STKEGGGFYA DDTAGWDTRI
3060 3070 3080 3090 3100
TEADLDDEQE IMSYMNAEQR KLAWAVMEMT YKNKVVKVLR PAPGGKAFMD
3110 3120 3130 3140 3150
IISRRDQRGS GQVVTYALNT ITNLKVQLIR MAEAEMVINH QHVNECDEGV
3160 3170 3180 3190 3200
LARLDAWLAE NGCDRLARMA VSGDDCVVRP VDDRFGLALS HLNAMSKVRK
3210 3220 3230 3240 3250
DISEWQPSKE WTDWENVPFC SHHFHELVLK DGRKVVVPCR DQDELIGRGR
3260 3270 3280 3290 3300
VSPGNGWMIK ETACLSKAYA NMWSLMYFHK RDMRLLSFAV SSAVPMAWVP
3310 3320 3330 3340 3350
SGRTTWSVHG KGEWMTTQDM LDVWNRVWVL NNPHMKDKTT VKEWRDVPYL
3360 3370 3380 3390 3400
TKRQDKLCGS LIGMTNRATW ASHIHLVIHR IRTLIGQEKY TDYLTVMDRY
3410
SVDADLQPGE LI
Length:3,412
Mass (Da):378,659
Last modified:October 31, 2006 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD05565AA63487306
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
DQ235229 Genomic RNA Translation: ABB69689.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ235229 Genomic RNA Translation: ABB69689.1

3D structure databases

SMRiQ074N0
ModBaseiSearch...

Proteomic databases

PRIDEiQ074N0

Family and domain databases

CDDicd12149 Flavi_E_C, 1 hit
Gene3Di1.10.8.970, 1 hit
1.20.1280.260, 1 hit
2.60.260.50, 1 hit
2.60.40.350, 1 hit
2.60.98.10, 1 hit
3.30.387.10, 1 hit
3.30.67.10, 1 hit
InterProiView protein in InterPro
IPR011492 DEAD_Flavivir
IPR000069 Env_glycoprot_M_flavivir
IPR038302 Env_glycoprot_M_sf_flavivir
IPR013755 Flav_gly_cen_dom_subdom1
IPR001122 Flavi_capsidC
IPR027287 Flavi_E_Ig-like
IPR026470 Flavi_E_Stem/Anchor_dom
IPR038345 Flavi_E_Stem/Anchor_dom_sf
IPR001157 Flavi_NS1
IPR000752 Flavi_NS2A
IPR000487 Flavi_NS2B
IPR000404 Flavi_NS4A
IPR001528 Flavi_NS4B
IPR002535 Flavi_propep
IPR038688 Flavi_propep_sf
IPR000336 Flavivir/Alphavir_Ig-like_sf
IPR001850 Flavivirus_NS3_S7
IPR014412 Gen_Poly_FLV
IPR011998 Glycoprot_cen/dimer
IPR036253 Glycoprot_cen/dimer_sf
IPR038055 Glycoprot_E_dimer_dom
IPR013756 GlyE_cen_dom_subdom2
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR014756 Ig_E-set
IPR026490 mRNA_cap_0/1_MeTrfase
IPR027417 P-loop_NTPase
IPR009003 Peptidase_S1_PA
IPR000208 RNA-dir_pol_flavivirus
IPR007094 RNA-dir_pol_PSvirus
IPR002877 rRNA_MeTrfase_FtsJ_dom
IPR029063 SAM-dependent_MTases
PfamiView protein in Pfam
PF01003 Flavi_capsid, 1 hit
PF07652 Flavi_DEAD, 1 hit
PF02832 Flavi_glycop_C, 1 hit
PF00869 Flavi_glycoprot, 1 hit
PF01004 Flavi_M, 1 hit
PF00948 Flavi_NS1, 1 hit
PF01005 Flavi_NS2A, 1 hit
PF01002 Flavi_NS2B, 1 hit
PF01350 Flavi_NS4A, 1 hit
PF01349 Flavi_NS4B, 1 hit
PF00972 Flavi_NS5, 1 hit
PF01570 Flavi_propep, 1 hit
PF01728 FtsJ, 1 hit
PF00949 Peptidase_S7, 1 hit
PIRSFiPIRSF003817 Gen_Poly_FLV, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 2 hits
SSF53335 SSF53335, 1 hit
SSF56983 SSF56983, 1 hit
SSF81296 SSF81296, 1 hit
TIGRFAMsiTIGR04240 flavi_E_stem, 1 hit
PROSITEiView protein in PROSITE
PS51527 FLAVIVIRUS_NS2B, 1 hit
PS51528 FLAVIVIRUS_NS3PRO, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit
PS51591 RNA_CAP01_NS5_MT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOLG_YEFVE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q074N0
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: October 31, 2006
Last modified: September 18, 2019
This is version 103 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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